| UniProt ID | POB3_YEAST | |
|---|---|---|
| UniProt AC | Q04636 | |
| Protein Name | FACT complex subunit POB3 | |
| Gene Name | POB3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 552 | |
| Subcellular Localization | Nucleus . Chromosome . Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. | |
| Protein Description | Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Transcription elongation is promoted by the repression of transcription initiation from cryptic sites. Also acts in establishing transcription initiation complexes and promotes SPT15/TBP-binding to a TATA box. Together with replication factor-A protein (RPA), FACT may play a role in nucleosome deposition during DNA replication.. | |
| Protein Sequence | MSTDFDRIYLNQSKFSGRFRIADSGLGWKISTSGGSAANQARKPFLLPATELSTVQWSRGCRGYDLKINTKNQGVIQLDGFSQDDYNLIKNDFHRRFNIQVEQREHSLRGWNWGKTDLARNEMVFALNGKPTFEIPYARINNTNLTSKNEVGIEFNIQDEEYQPAGDELVEMRFYIPGVIQTNVDENMTKKEESSNEVVPKKEDGAEGEDVQMAVEEKSMAEAFYEELKEKADIGEVAGDAIVSFQDVFFTTPRGRYDIDIYKNSIRLRGKTYEYKLQHRQIQRIVSLPKADDIHHLLVLAIEPPLRQGQTTYPFLVLQFQKDEETEVQLNLEDEDYEENYKDKLKKQYDAKTHIVLSHVLKGLTDRRVIVPGEYKSKYDQCAVSCSFKANEGYLYPLDNAFFFLTKPTLYIPFSDVSMVNISRAGQTSTSSRTFDLEVVLRSNRGSTTFANISKEEQQLLEQFLKSKNLRVKNEDREVQERLQTALGSDSDEEDINMGSAGEDDESVDEDFQVSSDNDADEVAEEFDSDAALSDAEGGSDEERPSKKPKVE | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 14 | Acetylation | RIYLNQSKFSGRFRI EEEECCCCCCCCEEE | 33.51 | 24489116 | |
| 29 | Acetylation | ADSGLGWKISTSGGS CCCCCCEEEECCCCC | 25.61 | 24489116 | |
| 31 | Phosphorylation | SGLGWKISTSGGSAA CCCCEEEECCCCCHH | 16.88 | 22369663 | |
| 32 | Phosphorylation | GLGWKISTSGGSAAN CCCEEEECCCCCHHH | 34.56 | 22369663 | |
| 33 | Phosphorylation | LGWKISTSGGSAANQ CCEEEECCCCCHHHH | 34.07 | 22369663 | |
| 36 | Phosphorylation | KISTSGGSAANQARK EEECCCCCHHHHCCC | 27.94 | 22369663 | |
| 43 | Ubiquitination | SAANQARKPFLLPAT CHHHHCCCCCCCCCH | 43.04 | 17644757 | |
| 43 | Acetylation | SAANQARKPFLLPAT CHHHHCCCCCCCCCH | 43.04 | 24489116 | |
| 67 | Acetylation | GCRGYDLKINTKNQG CCCCEEEEEEECCCC | 30.89 | 25381059 | |
| 90 | Acetylation | QDDYNLIKNDFHRRF HHHHCHHHHHHHHHH | 54.34 | 24489116 | |
| 115 | Acetylation | LRGWNWGKTDLARNE CCCCCCCCCHHHHCE | 30.40 | 24489116 | |
| 132 | Phosphorylation | FALNGKPTFEIPYAR EEECCCEEEECCEEE | 37.07 | 19779198 | |
| 146 | Phosphorylation | RINNTNLTSKNEVGI EECCCCCCCCCEEEE | 39.46 | 19779198 | |
| 147 | Phosphorylation | INNTNLTSKNEVGIE ECCCCCCCCCEEEEE | 36.33 | 19779198 | |
| 191 | Ubiquitination | VDENMTKKEESSNEV CCCCCCCCCHHCCCC | 58.51 | 23749301 | |
| 194 | Phosphorylation | NMTKKEESSNEVVPK CCCCCCHHCCCCCCC | 39.28 | 17287358 | |
| 195 | Phosphorylation | MTKKEESSNEVVPKK CCCCCHHCCCCCCCC | 40.05 | 17287358 | |
| 229 | Acetylation | EAFYEELKEKADIGE HHHHHHHHHHCCCCH | 61.52 | 25381059 | |
| 352 | Ubiquitination | LKKQYDAKTHIVLSH HHHHHHHHHHHHHHH | 37.42 | 17644757 | |
| 362 | Ubiquitination | IVLSHVLKGLTDRRV HHHHHHHCCCCCCEE | 51.27 | 17644757 | |
| 376 | Ubiquitination | VIVPGEYKSKYDQCA EECCCCCCCCCCCCE | 35.85 | 17644757 | |
| 378 | Acetylation | VPGEYKSKYDQCAVS CCCCCCCCCCCCEEE | 49.01 | 25381059 | |
| 378 | Ubiquitination | VPGEYKSKYDQCAVS CCCCCCCCCCCCEEE | 49.01 | 17644757 | |
| 389 | Ubiquitination | CAVSCSFKANEGYLY CEEEEEEECCCCEEE | 33.73 | 17644757 | |
| 430 | Phosphorylation | SRAGQTSTSSRTFDL ECCCCCCCCCCEEEE | 33.82 | 27214570 | |
| 432 | Phosphorylation | AGQTSTSSRTFDLEV CCCCCCCCCEEEEEE | 35.11 | 25752575 | |
| 447 | Phosphorylation | VLRSNRGSTTFANIS EEECCCCCCCCCCCC | 22.49 | 28889911 | |
| 455 | Ubiquitination | TTFANISKEEQQLLE CCCCCCCHHHHHHHH | 62.57 | 17644757 | |
| 466 | Acetylation | QLLEQFLKSKNLRVK HHHHHHHHHCCCCCC | 61.75 | 24489116 | |
| 466 | Ubiquitination | QLLEQFLKSKNLRVK HHHHHHHHHCCCCCC | 61.75 | 17644757 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of POB3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of POB3_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of POB3_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-195, ANDMASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-195, ANDMASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-195, ANDMASS SPECTROMETRY. | |
